Reviewed, UniProtKB/Swiss-Prot Q944B6 (TYRA1_ARATH)

Names and origin

Protein names

Recommended name:
    Arogenate dehydrogenase 1, chloroplastic
    EC=1.3.1.78
Alternative name(s):
    TyrAAT1
    TYRATC

Gene names

Name:	TYRAAT1
Ordered Locus Names:	At5g34930
ORF Names:	T2L5.1

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	640 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the biosynthesis of tyrosine. Has no prephenate dehydrogenase activity. Ref.4
Catalytic activity	L-arogenate + NADP+ = L-tyrosine + NADPH + CO2.
Pathway	Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from L-arogenate: step 1/1.
Subcellular location	Plastid › chloroplast Potential.
Tissue specificity	Expressed in roots, stems, leaves, flowers, siliques and seeds. More abundant in seeds.
Induction	Strongly inhibited by tyrosine. Ref.1
Miscellaneous	Unlike TYRAAT2, TYRAAT1 is composed of two highly similar and catalytically active peptide domains. No proteolytic cleavage between the two domains.
Sequence similarities	Contains 2 prephenate/arogenate dehydrogenase domains.
biophysicochemical properties	Kinetic parameters: NADP increases the apparent affinity for arogenate. The two active domains have the same KM values for arogenate. KM=10.2 µM for NADP KM=52.6 µM for arogenate Vmax=142 µmol/min/mg enzyme
Sequence caution	The sequence AAC62791.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAB10786.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tyrosine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Repeat Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tyrosine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arogenate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro prephenate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 18	18	Chloroplast Potential
	Chain	19 – 640	622	Arogenate dehydrogenase 1, chloroplastic		PRO_0000269677
Regions
	Domain	53 – 334	282	Prephenate/arogenate dehydrogenase 1
	Domain	365 – 640	276	Prephenate/arogenate dehydrogenase 2

Sequences

	Sequence		Length	Mass (Da)
	Q944B6-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 3D9922F91B8FF810	FASTA	640	72,301
	10 20 30 40 50 60 MAETLITKPP LSLSFTSLSS MLPSLSLSTA NRHLSVTDTI PLPNSNSNAT PPLRIAIIGF 70 80 90 100 110 120 GNYGQFLAET LISQGHILFA HSRSDHSSAA RRLGVSYFTD LHDLCERHPD VVLLCTSILS 130 140 150 160 170 180 IENILKTLPF QRLRRNTLFV DVLSVKEFAK TLLLQYLPED FDILCTHPMF GPQSVSSNHG 190 200 210 220 230 240 WRGLRFVYDK VRIGEERLRV SRCESFLEIF VREGCEMVEM SVTDHDKFAA ESQFITHTLG 250 260 270 280 290 300 RLLGMLKLIS TPINTKGYEA LLDLAENICG DSFDLYYGLF VYNNNSLEVL ERIDLAFEAL 310 320 330 340 350 360 RKELFSRLHG VVRKQSFEGE AKKVHVFPNC GENDASLDMM RSEDVVVKYE YNSQVSGSVN 370 380 390 400 410 420 DGSRLKIGIV GFGNFGQFLG KTMVKQGHTV LAYSRSDYTD EAAKLGVSYF SDLDDLFEEH 430 440 450 460 470 480 PEVIILCTSI LSTEKVLESL PFQRLKRSTL FVDVLSVKEF PRNLFLQTLP QDFDILCTHP 490 500 510 520 530 540 MFGPESGKNG WNNLAFVFDK VRIGMDDRRK SRCNSFLDIF AREGCRMVEM SCAEHDWHAA 550 560 570 580 590 600 GSQFITHTVG RLLEKLSLES TPIDTKGYET LLKLVENTAG DSFDLYYGLF LYNPNAMEQL 610 620 630 640 ERFHVAFESL KTQLFGRLHS QHSHELAKSS SPKTTKLLTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase with two highly similar and active protein domains." Rippert P., Matringe M. Plant Mol. Biol. 48:361-368(2002) [PubMed: 11905963] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. XI." Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana." Rippert P., Matringe M. Eur. J. Biochem. 269:4753-4761(2002) [PubMed: 12354106] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[5]	"Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis." Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M. Plant Physiol. 149:1251-1260(2009) [PubMed: 19136569] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, LACK OF PROCESSING.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF434681 mRNA. Translation: AAL30405.1. AF096371 Genomic DNA. Translation: AAC62791.1. Sequence problems. AB028613 Genomic DNA. Translation: BAB10786.1. Sequence problems.
IPI	IPI00533992.
PIR	T01952.
RefSeq	NP_198343.1.
UniGene	At.1659
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q944B6.
Genome annotation databases
GeneID	833436.
GenomeReviews	Gene locus AT5G34930 in contig BA000015_GR.
KEGG	ath:AT5G34930.
NMPDR	fig|3702.1.peg.25198.
Organism-specific databases
TAIR	At5g34930.
Enzyme and pathway databases
BRENDA	1.3.1.78. 302.
Family and domain databases
InterPro	IPR016040. NAD(P)-bd_dom. IPR004455. NADP_OxRdtase_F420. IPR003099. Prephen_DH. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF03807. F420_oxidored. 1 hit. PF02153. PDH. 1 hit. [Graphical view]
PROSITE	PS51176. PDH_ADH. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TYRA1_ARATH

Accession

Primary (citable) accession number: Q944B6
Secondary accession number(s): O82603

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)